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. 1993 Aug 15;90(16):7508–7512. doi: 10.1073/pnas.90.16.7508

Amyloid beta-protein activates tachykinin receptors and inositol trisphosphate accumulation by synergy with glutamate.

H Kimura 1, D Schubert 1
PMCID: PMC47171  PMID: 7689220

Abstract

The biological function of the soluble form of the amyloid beta-protein (ABP) was examined by assaying its interaction with neuronal receptors expressed in Xenopus oocytes. ABP weakly activated tachykinin receptors, but in the presence of N-methyl-D-aspartate and alpha-amino-3-hydroxy-5-methylisoxazole-4- propionate-type glutamate receptors ABP-induced responses were greatly enhanced. Glutamate and ABP together also induced accumulation of inositol trisphosphate and increases in intracellular Ca2+. These observations suggest that in the presence of glutamate, ABP can activate tachykinin receptors and phosphatidylinositol turnover. ABP may therefore act as a neuromodulatory peptide.

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Selected References

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